FMO DATABASE

FMODB ID: 668QZ

Calculation Name: 2HSN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2HSN

Chain ID: A

ChEMBL ID:

UniProt ID: P46672

Base Structure: X-ray

Registration Date: 2023-06-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	160
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1303747.679873
FMO2-HF: Nuclear repulsion	1240860.962393
FMO2-HF: Total energy	-62886.71748
FMO2-MP2: Total energy	-63072.915019

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:3:MET)

Summations of interaction energy for fragment #1(A:3:MET)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-14.598	-5.796	3.305	-4.13	-7.976	-0.009

Interaction energy analysis for fragmet #1(A:3:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / q_NPA : -0.010

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	5	PHE	0	-0.055	-0.014	3.031	-3.584	0.129	0.445	-1.874	-2.284	0.014
4	A	6	LEU	0	0.057	0.044	4.274	-1.423	-1.192	0.000	-0.036	-0.194	0.000
5	A	7	ILE	0	-0.024	-0.011	7.103	0.229	0.229	0.000	0.000	0.000	0.000
6	A	8	SER	0	0.038	0.003	9.254	-0.134	-0.134	0.000	0.000	0.000	0.000
7	A	9	PHE	0	-0.012	-0.016	12.872	0.036	0.036	0.000	0.000	0.000	0.000
8	A	10	ASP	-1	-0.804	-0.886	16.019	0.009	0.009	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.928	0.957	16.849	0.088	0.088	0.000	0.000	0.000	0.000
10	A	12	SER	0	-0.071	-0.026	21.263	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	13	LYS	1	1.005	1.040	21.590	-0.021	-0.021	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.904	0.942	24.590	0.011	0.011	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.033	-0.041	22.319	0.009	0.009	0.000	0.000	0.000	0.000
14	A	16	PRO	0	0.029	0.000	27.041	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	17	ALA	0	0.072	0.040	27.195	0.000	0.000	0.000	0.000	0.000	0.000
16	A	18	HIS	0	0.065	0.020	26.592	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.032	-0.017	23.529	0.000	0.000	0.000	0.000	0.000	0.000
18	A	20	GLN	0	0.003	0.011	22.518	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	21	LEU	0	0.019	0.021	21.601	-0.004	-0.004	0.000	0.000	0.000	0.000
20	A	22	ALA	0	0.002	0.002	21.868	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	23	ASN	0	-0.048	-0.041	18.914	0.004	0.004	0.000	0.000	0.000	0.000
22	A	24	ASN	0	0.034	0.001	17.478	0.003	0.003	0.000	0.000	0.000	0.000
23	A	25	LEU	0	0.007	0.011	17.398	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	26	LYS	1	0.944	0.970	16.769	-0.020	-0.020	0.000	0.000	0.000	0.000
25	A	27	ILE	0	0.003	0.003	12.185	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	28	ALA	0	0.019	0.003	12.634	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	29	LEU	0	0.003	-0.001	14.064	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	30	ALA	0	-0.007	0.004	10.445	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	31	LEU	0	-0.002	-0.003	8.317	-0.085	-0.085	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.935	-0.971	10.341	-0.230	-0.230	0.000	0.000	0.000	0.000
31	A	33	TYR	0	-0.049	-0.021	12.686	0.006	0.006	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.017	0.015	7.186	-0.011	-0.011	0.000	0.000	0.000	0.000
33	A	35	SER	0	0.018	-0.009	7.669	0.035	0.035	0.000	0.000	0.000	0.000
34	A	36	LYS	1	0.916	0.979	4.946	-0.186	-0.186	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.016	-0.027	2.422	-1.638	-0.370	1.522	-0.949	-1.841	-0.007
36	A	38	LEU	0	-0.016	0.004	2.740	-2.093	-1.484	1.121	-0.171	-1.559	-0.009
37	A	39	LYS	1	0.858	0.930	2.985	1.108	1.983	0.039	-0.214	-0.699	0.000
38	A	40	PRO	0	-0.045	-0.015	2.945	-3.802	-1.900	0.178	-0.853	-1.228	-0.007
39	A	41	GLU	-1	-0.898	-0.933	3.885	-2.305	-2.101	0.000	-0.033	-0.171	0.000
40	A	42	VAL	0	-0.023	-0.025	5.422	0.533	0.533	0.000	0.000	0.000	0.000
41	A	43	ASP	-1	-0.860	-0.933	9.149	-0.219	-0.219	0.000	0.000	0.000	0.000
42	A	44	ASN	0	-0.069	-0.053	11.407	0.066	0.066	0.000	0.000	0.000	0.000
43	A	45	ASP	-1	-0.925	-0.960	15.053	-0.075	-0.075	0.000	0.000	0.000	0.000
44	A	46	ASN	0	0.085	0.064	14.338	0.013	0.013	0.000	0.000	0.000	0.000
45	A	47	ALA	0	-0.033	-0.030	16.711	-0.009	-0.009	0.000	0.000	0.000	0.000
46	A	48	ALA	0	-0.038	-0.021	18.298	0.004	0.004	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.034	0.010	15.205	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.896	-0.953	12.758	0.161	0.161	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.011	-0.010	6.570	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	52	ARG	1	0.925	0.967	9.106	-0.125	-0.125	0.000	0.000	0.000	0.000
51	A	53	ASN	0	0.015	-0.008	7.189	0.399	0.399	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.042	-0.040	6.175	-0.557	-0.557	0.000	0.000	0.000	0.000
53	A	55	LYS	1	0.896	0.950	6.278	-0.638	-0.638	0.000	0.000	0.000	0.000
54	A	56	GLU	-1	-0.878	-0.928	9.684	-0.066	-0.066	0.000	0.000	0.000	0.000
55	A	57	PRO	0	-0.035	-0.006	13.261	0.049	0.049	0.000	0.000	0.000	0.000
56	A	58	PHE	0	-0.020	-0.019	16.050	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	59	LEU	0	-0.007	-0.005	18.578	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	60	LEU	0	-0.004	0.006	20.959	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.029	0.002	21.291	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	62	ASP	-1	-0.869	-0.927	24.963	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.039	0.005	27.923	0.003	0.003	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.001	-0.008	31.175	0.002	0.002	0.000	0.000	0.000	0.000
63	A	65	ALA	0	0.002	-0.010	27.321	0.002	0.002	0.000	0.000	0.000	0.000
64	A	66	ILE	0	-0.015	0.000	27.418	0.003	0.003	0.000	0.000	0.000	0.000
65	A	67	LEU	0	-0.027	-0.012	29.601	0.002	0.002	0.000	0.000	0.000	0.000
66	A	68	ARG	1	0.848	0.900	31.437	-0.009	-0.009	0.000	0.000	0.000	0.000
67	A	69	TYR	0	-0.015	0.009	25.042	0.002	0.002	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.073	-0.040	30.102	0.002	0.002	0.000	0.000	0.000	0.000
69	A	71	MET	0	-0.093	-0.041	32.123	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.942	-0.960	32.205	0.025	0.025	0.000	0.000	0.000	0.000
71	A	73	ASP	-1	-0.829	-0.901	33.216	0.012	0.012	0.000	0.000	0.000	0.000
72	A	74	PHE	0	0.015	-0.014	28.955	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.868	-0.917	33.770	0.014	0.014	0.000	0.000	0.000	0.000
74	A	76	GLY	0	-0.026	-0.023	37.218	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	77	GLN	0	-0.026	-0.037	30.979	0.000	0.000	0.000	0.000	0.000	0.000
76	A	78	THR	0	0.029	0.011	36.249	0.000	0.000	0.000	0.000	0.000	0.000
77	A	79	SER	0	-0.073	-0.032	38.172	0.000	0.000	0.000	0.000	0.000	0.000
78	A	80	ASP	-1	-0.846	-0.914	40.690	0.005	0.005	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.884	0.923	43.031	-0.007	-0.007	0.000	0.000	0.000	0.000
80	A	82	TYR	0	0.021	0.008	33.115	0.000	0.000	0.000	0.000	0.000	0.000
81	A	83	GLN	0	0.074	0.030	35.531	0.000	0.000	0.000	0.000	0.000	0.000
82	A	84	PHE	0	-0.019	-0.001	39.272	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.026	0.003	39.298	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	86	LEU	0	-0.025	-0.015	33.900	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	87	ALA	0	-0.014	-0.013	36.969	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	SER	0	-0.080	-0.029	38.448	0.000	0.000	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.007	0.004	40.927	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	GLN	0	0.062	0.034	33.037	0.000	0.000	0.000	0.000	0.000	0.000
89	A	91	ASN	0	0.030	0.006	36.320	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.005	-0.005	37.378	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.021	-0.006	37.083	-0.001	-0.001	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.037	-0.003	31.121	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	95	HIS	0	-0.070	-0.022	36.183	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	LYS	1	0.936	0.954	36.379	0.015	0.015	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.930	-0.952	39.826	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	98	LEU	0	0.010	0.002	42.128	0.000	0.000	0.000	0.000	0.000	0.000
97	A	99	PRO	0	-0.001	0.009	44.061	0.000	0.000	0.000	0.000	0.000	0.000
98	A	100	GLN	0	0.046	-0.002	47.202	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLN	0	0.038	0.023	49.824	0.000	0.000	0.000	0.000	0.000	0.000
100	A	102	HIS	0	0.007	-0.008	47.461	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.021	0.021	45.504	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.854	-0.891	47.864	0.000	0.000	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.006	-0.003	51.385	0.000	0.000	0.000	0.000	0.000	0.000
104	A	106	LEU	0	-0.050	-0.019	45.033	0.000	0.000	0.000	0.000	0.000	0.000
105	A	107	THR	0	0.017	-0.025	46.696	0.000	0.000	0.000	0.000	0.000	0.000
106	A	108	ASN	0	0.033	0.005	48.780	0.000	0.000	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.939	0.973	48.949	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	110	ALA	0	-0.015	0.002	46.711	0.000	0.000	0.000	0.000	0.000	0.000
109	A	111	ILE	0	-0.066	-0.036	48.536	0.000	0.000	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.950	-0.938	51.214	0.003	0.003	0.000	0.000	0.000	0.000
111	A	113	ASN	0	-0.044	-0.043	49.878	0.000	0.000	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.045	-0.022	46.382	0.000	0.000	0.000	0.000	0.000	0.000
113	A	115	LEU	0	-0.024	-0.019	46.750	0.000	0.000	0.000	0.000	0.000	0.000
114	A	116	VAL	0	0.087	0.037	49.320	0.000	0.000	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.876	-0.918	50.134	0.006	0.006	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.018	-0.017	47.579	0.000	0.000	0.000	0.000	0.000	0.000
117	A	119	LYS	1	0.832	0.899	49.907	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	120	GLU	-1	-0.970	-0.917	47.479	0.007	0.007	0.000	0.000	0.000	0.000
119	A	121	PRO	0	0.047	-0.065	45.385	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	LEU	0	-0.038	0.007	44.207	0.000	0.000	0.000	0.000	0.000	0.000
121	A	123	THR	0	0.043	0.041	40.960	0.000	0.000	0.000	0.000	0.000	0.000
122	A	124	THR	0	0.052	0.011	36.156	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.017	-0.009	38.539	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	126	ASP	-1	-0.864	-0.914	39.705	0.006	0.006	0.000	0.000	0.000	0.000
125	A	127	LEU	0	-0.031	-0.017	39.874	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.006	0.011	35.210	-0.001	-0.001	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.024	-0.005	39.110	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	130	PHE	0	0.012	-0.011	42.161	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	131	ALA	0	-0.021	-0.006	39.648	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	132	ASN	0	-0.002	-0.008	37.724	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.008	0.002	41.266	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	TYR	0	-0.022	-0.012	44.251	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	135	ALA	0	-0.038	-0.029	41.398	0.000	0.000	0.000	0.000	0.000	0.000
134	A	136	LEU	0	-0.045	-0.013	42.244	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.036	-0.037	45.202	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	SER	0	0.050	0.027	47.960	0.000	0.000	0.000	0.000	0.000	0.000
137	A	139	SER	0	-0.024	0.004	49.578	0.000	0.000	0.000	0.000	0.000	0.000
138	A	140	LEU	0	0.074	0.043	51.108	0.000	0.000	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.001	-0.009	48.306	0.000	0.000	0.000	0.000	0.000	0.000
140	A	142	HIS	0	-0.068	-0.024	51.792	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.014	-0.011	54.313	0.000	0.000	0.000	0.000	0.000	0.000
142	A	144	LYS	1	0.840	0.958	53.047	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.044	-0.068	50.385	0.000	0.000	0.000	0.000	0.000	0.000
144	A	146	PRO	0	0.031	0.028	54.030	0.000	0.000	0.000	0.000	0.000	0.000
145	A	147	GLU	-1	-0.948	-0.964	55.548	0.002	0.002	0.000	0.000	0.000	0.000
146	A	148	LEU	0	-0.055	-0.026	49.075	0.000	0.000	0.000	0.000	0.000	0.000
147	A	149	PRO	0	0.090	0.042	48.504	0.000	0.000	0.000	0.000	0.000	0.000
148	A	150	SER	0	0.048	0.017	49.198	0.000	0.000	0.000	0.000	0.000	0.000
149	A	151	LYS	1	0.967	0.983	43.348	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	152	VAL	0	0.066	0.033	44.758	0.000	0.000	0.000	0.000	0.000	0.000
151	A	153	HIS	0	-0.012	0.002	45.826	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	154	ASN	0	-0.019	-0.030	45.230	-0.001	-0.001	0.000	0.000	0.000	0.000
153	A	155	ALA	0	-0.001	0.009	41.647	0.000	0.000	0.000	0.000	0.000	0.000
154	A	156	VAL	0	0.026	0.017	42.915	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	157	ALA	0	-0.028	-0.010	45.168	-0.001	-0.001	0.000	0.000	0.000	0.000
156	A	158	LEU	0	-0.074	-0.040	39.305	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	159	ALA	0	0.029	-0.004	40.801	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.932	0.984	41.756	0.000	0.000	0.000	0.000	0.000	0.000
159	A	161	LYS	1	0.891	0.960	43.980	0.001	0.001	0.000	0.000	0.000	0.000
160	A	162	HIS	0	0.022	0.021	41.128	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:MET)